Inhibition of nuclear factor kappaB proteins-platinated DNA interactions correlates with cytotoxic effectiveness of the platinum complexes

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F16%3A00470811" target="_blank" >RIV/68081707:_____/16:00470811 - isvavai.cz</a>

Alternative codes found

RIV/61989592:15310/16:33161145

Result on the web

<a href="http://dx.doi.org/10.1038/srep28474" target="_blank" >http://dx.doi.org/10.1038/srep28474</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/srep28474" target="_blank" >10.1038/srep28474</a>

Result language

angličtina

Original language name

Inhibition of nuclear factor kappaB proteins-platinated DNA interactions correlates with cytotoxic effectiveness of the platinum complexes

Original language description

Nuclear DNA is the target responsible for anticancer activity of platinum anticancer drugs. Their activity is mediated by altered signals related to programmed cell death and the activation of various signaling pathways. An example is activation of nuclear factor kappaB (NF-kappa B). Binding of NF-kappa B proteins to their consensus sequences in DNA (kappa B sites) is the key biochemical activity responsible for the biological functions of NF-kappa B. Using gel-mobility-shift assays and surface plasmon resonance spectroscopy we examined the interactions of NF-kappa B proteins with oligodeoxyribonucleotide duplexes containing kappa B site damaged by DNA adducts of three platinum complexes. These complexes markedly differed in their toxic effects in tumor cells and comprised highly cytotoxic trinuclear platinum(II) complex BBR3464, less cytotoxic conventional cisplatin and ineffective transplatin. The results indicate that structurally different DNA adducts of these platinum complexes exhibit a different efficiency to affect the affinity of the platinated DNA (kappa B sites) to NF-kappa B proteins. Our results support the hypothesis that structural perturbations induced in DNA by platinum(II) complexes correlate with their higher efficiency to inhibit binding of NF-kappa B proteins to their kappa B sites and cytotoxicity as well. However, the full generalization of this hypothesis will require to evaluate a larger series of platinum(II) complexes.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

BO - Biophysics

OECD FORD branch

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Project

<a href="/en/project/LH13096" target="_blank" >LH13096: Targeting DNA interactions with platinum anticancer drugs with damaged-DNA binding-proteins</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2016

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Scientific Reports

ISSN

2045-2322

e-ISSN

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Volume of the periodical

6

Issue of the periodical within the volume

AUG2016

Country of publishing house

GB - UNITED KINGDOM

Number of pages

12

Pages from-to

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UT code for WoS article

000382157100001

EID of the result in the Scopus database

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